Research workbench
GALPHAI3 co-crystallized with KB752
Analyse GALPHAI3 co-crystallized with KB752 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6MHE
- Type
- protein
- Length
- 342 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Guanine nucleotide-binding protein G(K) subunit alpha; KB752 peptide
- UniProt
- P08753
- Ligands
- GDP
- Pockets
- 3 · best druggability 0.66
Structure
x-ray diffraction · 2 distinct chains · 50% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Guanine nucleotide-binding protein G(K) subunit alpha | protein | 330 | 50% helix, 13% strand | P08753 |
| C | KB752 peptide | protein | 12 | 50% helix, 8% strand | — |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 378 | 0.66 | 0.80 | 48 | GDP |
| 2 | 198 | 0.53 | 0.78 | 26 | empty |
| 3 | 115 | 0.46 | 0.78 | 16 | empty |
Interfaces
1 interface between chains.
- A–C · 791 Ų buried · 13 hydrogen bonds · protein-protein
Compared structures
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P08753
- Elsewhere: RCSB PDB 6MHE · PDBe 6MHE · UniProt P08753
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